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UniProtKB - P11349 (NARH_ECOLI)

Protein

Respiratory nitrate reductase 1 beta chain

Gene

narH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi16Iron-sulfur 1 (4Fe-4S)2 Publications1
Metal bindingi19Iron-sulfur 1 (4Fe-4S)2 Publications1
Metal bindingi22Iron-sulfur 1 (4Fe-4S)2 Publications1
Metal bindingi26Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi184Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi187Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi192Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi196Iron-sulfur 4 (3Fe-4S)2 Publications1
Metal bindingi217Iron-sulfur 4 (3Fe-4S)2 Publications1
Metal bindingi223Iron-sulfur 4 (3Fe-4S)2 Publications1
Metal bindingi227Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi244Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi247Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi259Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi263Iron-sulfur 1 (4Fe-4S)2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • 3 iron, 4 sulfur cluster binding Source: EcoCyc
  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • electron transfer activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • nitrate reductase activity Source: EcoCyc
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • nitrate assimilation Source: UniProtKB-KW
  • nitrate metabolic process Source: EcoCyc
View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Nitrate assimilation, Transport
Ligand3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:NARH-MONOMER
MetaCyc:NARH-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.7.5.1 2026

Protein family/group databases

Transport Classification Database

More...TCDBi		5.A.3.1.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Respiratory nitrate reductase 1 beta chain (EC:1.7.5.1)
Alternative name(s):
Nitrate reductase A subunit beta
Quinol-nitrate oxidoreductase subunit beta
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:narH
Ordered Locus Names:b1225, JW1216
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10639 narH

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

Drug and drug target database

More...DrugBanki		DB04464 N-Formylmethionine

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000967201 – 512Respiratory nitrate reductase 1 beta chainAdd BLAST512

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P11349

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P11349

PRoteomics IDEntifications database

More...PRIDEi		P11349

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By nitrate.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4262231, 28 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1974 Nitrate reductase A complex

Database of interacting proteins

More...DIPi		DIP-10312N

Protein interaction database and analysis system

More...IntActi		P11349, 15 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_1284

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90B1-512[»]
1R27X-ray2.00B/D1-512[»]
1SIWX-ray2.20B1-512[»]
1Y4ZX-ray2.00B1-512[»]
1Y5IX-ray1.90B1-512[»]
1Y5LX-ray2.50B1-512[»]
1Y5NX-ray2.50B1-512[»]
3EGWX-ray1.90B1-509[»]
3IR5X-ray2.30B1-512[»]
3IR6X-ray2.80B1-512[»]
3IR7X-ray2.50B1-512[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P11349

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P11349

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P11349

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini7 – 354Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST29
Domaini175 – 2064Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32
Domaini208 – 2374Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4108IUE Bacteria
COG1140 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000237353

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P11349

KEGG Orthology (KO)

More...KOi		K00371

Database for complete collections of gene phylogenies

More...PhylomeDBi		P11349

Family and domain databases

Conserved Domains Database

More...CDDi		cd10557 NarH_beta-like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.3650.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR029263 Nitr_red_bet_C
IPR038262 Nitr_red_bet_C_sf
IPR006547 NO3_Rdtase_bsu

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13247 Fer4_11, 1 hit
PF14711 Nitr_red_bet_C, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01660 narH, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51379 4FE4S_FER_2, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P11349-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ 
        60         70         80         90        100
GFPTDWENQE KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY 
       110        120        130        140        150
YEPFDFDYQN LHTAPEGSKS QPIARPRSLI TGERMAKIEK GPNWEDDLGG 
       160        170        180        190        200
EFDKLAKDKN FDNIQKAMYS QFENTFMMYL PRLCEHCLNP ACVATCPSGA 
       210        220        230        240        250
IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK SEKCIFCYPR 
       260        270        280        290        300
IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF 
       310        320        330        340        350
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL 
       360        370        380        390        400
PMVWYVPPLS PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK 
       410        420        430        440        450
PVLRALKRML AMRHYKRAET VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA 
       460        470        480        490        500
NYEDRFVVPS SHRELAREAF PEKNGCGFTF GDGCHGSDTK FNLFNSRRID 
       510 
AIDVTSKTEP HP
Length:512
Mass (Da):58,066
Last modified:February 1, 1996 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2E7719C8D078BAEA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti398 – 417DTKPV…RHYKR → EYQTGTARTETYAGDASLQT in AAA24195 (PubMed:2832376).CuratedAdd BLAST20

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M20147 Genomic DNA Translation: AAA24195.1
U00096 Genomic DNA Translation: AAC74309.1
AP009048 Genomic DNA Translation: BAA36095.1
X16181 Genomic DNA Translation: CAA34304.1

Protein sequence database of the Protein Information Resource

More...PIRi		F64869 RDECNB

NCBI Reference Sequences

More...RefSeqi		NP_415743.1, NC_000913.3
WP_000702650.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74309; AAC74309; b1225
BAA36095; BAA36095; BAA36095

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945780

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1216
eco:b1225

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1056

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20147 Genomic DNA Translation: AAA24195.1
U00096 Genomic DNA Translation: AAC74309.1
AP009048 Genomic DNA Translation: BAA36095.1
X16181 Genomic DNA Translation: CAA34304.1
PIRiF64869 RDECNB
RefSeqiNP_415743.1, NC_000913.3
WP_000702650.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90B1-512[»]
1R27X-ray2.00B/D1-512[»]
1SIWX-ray2.20B1-512[»]
1Y4ZX-ray2.00B1-512[»]
1Y5IX-ray1.90B1-512[»]
1Y5LX-ray2.50B1-512[»]
1Y5NX-ray2.50B1-512[»]
3EGWX-ray1.90B1-509[»]
3IR5X-ray2.30B1-512[»]
3IR6X-ray2.80B1-512[»]
3IR7X-ray2.50B1-512[»]
ProteinModelPortaliP11349
SMRiP11349
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262231, 28 interactors
ComplexPortaliCPX-1974 Nitrate reductase A complex
DIPiDIP-10312N
IntActiP11349, 15 interactors
STRINGi316385.ECDH10B_1284

Chemistry databases

DrugBankiDB04464 N-Formylmethionine

Protein family/group databases

TCDBi5.A.3.1.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

Proteomic databases

jPOSTiP11349
PaxDbiP11349
PRIDEiP11349

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74309; AAC74309; b1225
BAA36095; BAA36095; BAA36095
GeneIDi945780
KEGGiecj:JW1216
eco:b1225
PATRICifig|1411691.4.peg.1056

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0633
EcoGeneiEG10639 narH

Phylogenomic databases

eggNOGiENOG4108IUE Bacteria
COG1140 LUCA
HOGENOMiHOG000237353
InParanoidiP11349
KOiK00371
PhylomeDBiP11349

Enzyme and pathway databases

BioCyciEcoCyc:NARH-MONOMER
MetaCyc:NARH-MONOMER
BRENDAi1.7.5.1 2026

Miscellaneous databases

EvolutionaryTraceiP11349

Protein Ontology

More...PROi		PR:P11349

Family and domain databases

CDDicd10557 NarH_beta-like, 1 hit
Gene3Di1.10.3650.10, 1 hit
InterProiView protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR029263 Nitr_red_bet_C
IPR038262 Nitr_red_bet_C_sf
IPR006547 NO3_Rdtase_bsu
PfamiView protein in Pfam
PF13247 Fer4_11, 1 hit
PF14711 Nitr_red_bet_C, 1 hit
TIGRFAMsiTIGR01660 narH, 1 hit
PROSITEiView protein in PROSITE
PS51379 4FE4S_FER_2, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNARH_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P11349
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1996
Last modified: January 16, 2019
This is version 180 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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